ID   I3TSB4_TISMK            Unreviewed;       339 AA.
AC   I3TSB4;
DT   05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2012, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   RecName: Full=Aldose 1-epimerase {ECO:0000256|PIRNR:PIRNR005096};
DE            EC=5.1.3.3 {ECO:0000256|PIRNR:PIRNR005096};
GN   OrderedLocusNames=TMO_a0249 {ECO:0000313|EMBL:AFK55652.1};
OS   Tistrella mobilis (strain KA081020-065).
OG   Plasmid pTM1 {ECO:0000313|EMBL:AFK55652.1,
OG   ECO:0000313|Proteomes:UP000005258}.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Geminicoccales;
OC   Geminicoccaceae; Tistrella.
OX   NCBI_TaxID=1110502 {ECO:0000313|EMBL:AFK55652.1, ECO:0000313|Proteomes:UP000005258};
RN   [1] {ECO:0000313|EMBL:AFK55652.1, ECO:0000313|Proteomes:UP000005258}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KA081020-065 {ECO:0000313|Proteomes:UP000005258};
RC   PLASMID=Plasmid pTM1 {ECO:0000313|Proteomes:UP000005258};
RX   PubMed=22458477; DOI=10.1021/ja301735a;
RA   Xu Y., Kersten R.D., Nam S.J., Lu L., Al-Suwailem A.M., Zheng H.,
RA   Fenical W., Dorrestein P.C., Moore B.S., Qian P.Y.;
RT   "Bacterial biosynthesis and maturation of the didemnin anti-cancer
RT   agents.";
RL   J. Am. Chem. Soc. 134:8625-8632(2012).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=alpha-D-glucose = beta-D-glucose; Xref=Rhea:RHEA:10264,
CC         ChEBI:CHEBI:15903, ChEBI:CHEBI:17925; EC=5.1.3.3;
CC         Evidence={ECO:0000256|PIRNR:PIRNR005096};
CC   -!- PATHWAY: Carbohydrate metabolism; hexose metabolism.
CC       {ECO:0000256|ARBA:ARBA00005028, ECO:0000256|PIRNR:PIRNR005096}.
CC   -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- SIMILARITY: Belongs to the aldose epimerase family.
CC       {ECO:0000256|ARBA:ARBA00006206, ECO:0000256|PIRNR:PIRNR005096}.
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DR   EMBL; CP003237; AFK55652.1; -; Genomic_DNA.
DR   AlphaFoldDB; I3TSB4; -.
DR   KEGG; tmo:TMO_a0249; -.
DR   PATRIC; fig|1110502.3.peg.3902; -.
DR   HOGENOM; CLU_031753_1_0_5; -.
DR   UniPathway; UPA00242; -.
DR   Proteomes; UP000005258; Plasmid pTM1.
DR   GO; GO:0004034; F:aldose 1-epimerase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0019318; P:hexose metabolic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd09019; galactose_mutarotase_like; 1.
DR   Gene3D; 2.70.98.10; -; 1.
DR   InterPro; IPR015443; Aldose_1-epimerase.
DR   InterPro; IPR008183; Aldose_1/G6P_1-epimerase.
DR   InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR   InterPro; IPR047215; Galactose_mutarotase-like.
DR   InterPro; IPR014718; GH-type_carb-bd.
DR   PANTHER; PTHR10091; ALDOSE-1-EPIMERASE; 1.
DR   PANTHER; PTHR10091:SF0; GALACTOSE MUTAROTASE; 1.
DR   Pfam; PF01263; Aldose_epim; 1.
DR   PIRSF; PIRSF005096; GALM; 1.
DR   SUPFAM; SSF74650; Galactose mutarotase-like; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|PIRNR:PIRNR005096};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|PIRNR:PIRNR005096};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Plasmid {ECO:0000313|EMBL:AFK55652.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005258}.
FT   ACT_SITE        171
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005096-1"
FT   ACT_SITE        303
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005096-1"
FT   BINDING         73..74
FT                   /ligand="beta-D-galactose"
FT                   /ligand_id="ChEBI:CHEBI:27667"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005096-3"
FT   BINDING         171..173
FT                   /ligand="beta-D-galactose"
FT                   /ligand_id="ChEBI:CHEBI:27667"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005096-3"
FT   BINDING         238
FT                   /ligand="beta-D-galactose"
FT                   /ligand_id="ChEBI:CHEBI:27667"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005096-2"
SQ   SEQUENCE   339 AA;  36407 MW;  84E90496A5DF1099 CRC64;
     MSGFGALPTG EIVERVEIAA HGLTARFLTL GAILQDLRLD GVQHPLVLGF DRLEGYLAHP
     DLYFGAMVGR YANRIGHARA PVGGQIVQLD ANFRGRHLLH GGADGSSRRN WRIRAVAADR
     VSLTDRLPDG HMGFPGNLEV EVGFSIAPGP VLRIDVRATS DAETLCNFAH HSYLNLSGRP
     TIAGHRLKVA ADSYLPVDDD LIPTGERRPV TGTPFDLRRG VTLMQEALIP GAPAGGFDHN
     FCLADARGPI RPVAWLTAPE GRLTLTVETT EPGLQVYDGA MIAAGMPGLD GRPLAPHAGL
     ALEPQLWPDA PNHPGFPPAL LRPGEVYEQH TALAFTDMR
//